Two duplicated piscidin genes from gilthead seabream (Sparus aurata) with different roles in vitro and in vivo

From the discovery of pleurocidin in skin mucus of winter flounder, many new related sequences have been found, forming a fish-exclusive family of antimicrobial peptides (AMP) called piscidin. Their mature peptides have a broad-spectrum antimicrobial activity and can be involved in the innate immune response. In the present work, two paralogous tripartite piscidin genes are formally described for the first time in gilthead seabream (Sparus aurata), an important marine farmed fish. Gene synteny and protein phylogeny clearly indicated a massive pisc gene expansion in a cluster of the chromosome 22 as well as a special evolution of piscidin in gilthead seabream compared to the rest of piscidins studied in other fish species. Despite being highly similar genes, they show totally different expression patterns in tissues and head-kidney leucocytes under both naïve and Vibrio/nodavirus-stimulated conditions. Moreover, these paralogous genes coded very different proteins according to their physicochemical properties. In this way, these piscidin genes have distinct roles not only related to their microbicide activity but also to their immune modulation. In addition, the present study improves the knowledge of duplication of AMP genes and adaptative diversification of teleost immune system.